Journal
FEBS JOURNAL
Volume 289, Issue 13, Pages 3813-3825Publisher
WILEY
DOI: 10.1111/febs.16239
Keywords
crystal structure; nanobodies; nucleocapsid protein; SARS-CoV-2
Categories
Funding
- National Natural Science Foundation of China [32022073, 31972287]
- Natural Science Foundation of Tianjin [19JCYBJC24500]
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The ongoing outbreak of COVID-19 caused by SARS-CoV-2 has posed a serious global public health threat. The crystal structures of the nucleocapsid protein C-terminal domain (CTD) have been reported, shedding light on the dimerization mechanism and RNA-binding site, and high-affinity sdAbs targeting different regions of the nucleocapsid protein have been identified, offering new possibilities for viral detection and therapeutic purposes.
The ongoing outbreak of COVID-19 caused by SARS-CoV-2 has resulted in a serious public health threat globally. Nucleocapsid protein is a major structural protein of SARS-CoV-2 that plays important roles in the viral RNA packing, replication, assembly, and infection. Here, we report two crystal structures of nucleocapsid protein C-terminal domain (CTD) at resolutions of 2.0 angstrom and 3.1 angstrom, respectively. These two structures, crystallized under different conditions, contain 2 and 12 CTDs in asymmetric unit, respectively. Interestingly, despite different crystal packing, both structures show a similar dimeric form as the smallest unit, consistent with its solution form measured by the size-exclusion chromatography, suggesting an important role of CTD in the dimerization of nucleocapsid proteins. By analyzing the surface charge distribution, we identified a stretch of positively charged residues between Lys257 and Arg262 that are involved in RNA-binding. Through screening a single-domain antibodies (sdAbs) library, we identified four sdAbs targeting different regions of nucleocapsid protein with high affinities that have future potential to be used in viral detection and therapeutic purposes.
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